Membrane topology of the 60-kDa Oxalp homologue from Escherichia coli

被引:77
作者
Sääf, A [1 ]
Monné, M [1 ]
de Gier, JW [1 ]
von Heijne, G [1 ]
机构
[1] Univ Stockholm, Dept Biochem, S-10691 Stockholm, Sweden
关键词
D O I
10.1074/jbc.273.46.30415
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We have characterized the membrane topology of a 60-kDa inner membrane protein from Escherichia coli that is homologous to the recently identified Oxalp protein in Saccharomyces cerevisiae mitochondria implicated in the assembly of mitochondrial inner membrane proteins. Hydrophobicity and alkaline phosphatase fusion analyses suggest a membrane topology with six transmembrane segments, including an N-terminal signal-anchor sequence not present in mitochondrial Oxalp. In contrast to partial N-terminal fusion protein constructs, the full-length protein folds into a protease-resistant conformation, suggesting that important folding determinants are present in the C-terminal part of the molecule.
引用
收藏
页码:30415 / 30418
页数:4
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